Studies of the structure and binding properties of hamster female protein.

We report here the characterization of hamster female protein (FP), a member of the pentraxin family of plasma proteins, as a molecule composed of glycosylated subunits of 25,655 MW containing a single intrachain disulphide bridge. In the presence of EDTA the subunits are non-covalently associated a...

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Autores principales: Tennent, G A, Baltz, M L, Osborn, G D, Butler, P J, Noble, G E, Hawkins, P N, Pepys, M B
Formato: Artigo
Lenguaje:Inglês
Publicado: 1993
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1422243/
https://ncbi.nlm.nih.gov/pubmed/7508422
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